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Sperm Signaling Specificity: From Sperm Maturation to Oocyte Recognition

  • Maria João Freitas
  • Daniela Patrício
  • Margarida FardilhaEmail author
Chapter
  • 70 Downloads

Abstract

The sperm cell is unique in its function. It is the only human cell that must leave the body where it is produced and fulfills its goal in a different organism being, thus, a highly specialized cell. Sperm cells are produced in the testis, acquire motility during the epididymis journey and fertilize the oocyte in the female reproductive system. Moreover, since these cells are virtually transcriptionally silent, they rely exclusively on protein-protein interactions and post translational modifications to control signaling pathways. These sperm cell unique features are reflected in sperm-specific signaling. Several sperm-specific/enriched proteins are responsible for controlling sperm functions such as sperm motility and acrosome reaction. In this chapter, we describe the signaling events that characterize sperm motility and acrosome reaction as well as the unique proteins that control such events.

Abbreviations

ADCY

Adenylyl cyclase

ADCY10

Adenylyl cyclase 10

AKAP4

A-Kinase anchor protein 4

AKT

Protein kinase B

ATP

Adenosine triphosphate

CarSper

Cation channel of sperm

DAG

Diacylglycerol

DNA

Deoxyribonucleic acid

GABA

Gamma aminobutyric acid

GAPDH

Lactate glyceraldehyde-3-phosphate dehydrogenase

GSK3

Glycogen synthase kinase 3

HPA

Human Protein Atlas

IP3

Inositol trisphosphate

LDH

Lactate dehydrogenase

LRP6

Low-density lipoprotein receptor-related protein 6

NGC

Nucleotide-gated channel

OAM

Outer acrosomal membrane

PDPK2

PDP kinase 2

PGK1

Phosphoglycerate kinase type 1

PIK3C

Phosphatidylinositol 3-kinase catalytic subunit

PIP2

Phosphatidylinositol 4,5-bisphosphate

PIP3

Phosphatidylinositol 3,4,5 trisphosphate

PLA2

Phospholipase A2

PLC

Phospholipase C

PLC

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase

PM

Plasma membrane

PPME1

Protein phosphatase methylesterase 1

PPP1

Phosphoprotein phosphatase 1

PPP1CC2

Phosphoprotein phosphatase 1 catalytic subunit C2

PPP1R11

Phosphoprotein phosphatase 1 regulatory subunit 11

PPP1R2

Phosphoprotein phosphatase 1 regulatory subunit 2

PPP1R2P3

PPP2CA pseudogene 3

PPP1R7

Phosphoprotein phosphatase 1 regulatory subunit 7

PPP2CA

Phosphoprotein phosphatase 2 catalytic subunit A

PR

Purinergic receptors

PRKA

cAMP-dependent protein kinase catalytic subunit alpha

PRKC

Protein kinase C

PTMs

Post-translational modifications

RyRs

Ryanodine receptors

SERCA

Sarcoplasmic-endoplasmic reticulum Ca2+ ATPase

SNARE

SNAP Receptor

SOC

Store-operated channels

TEX101

Testis-expressed protein 101

VOCCs

Voltage-dependent calcium channel

ZP

Zona pellucida

Notes

Acknowledgments

This work was financed by FEDER funds through the “Programa Operacional Competitividade e Internacionalização—COMPETE 2020” and by National Funds through the FCT—Fundação para a Ciência e Tecnologia (PTDB/BBB-BQB/3804/2014). We are thankful to Institute for Biomedicine—iBiMED (UID/BIM/04501/2013, POCI-01-0145-FEDER-007628 and UID/BIM/04501/2019) for supporting this project. iBiMED is supported by the Portuguese Foundation for Science and Technology (FCT), Compete2020 and FEDER fund. This work was also supported by an individual grant from FCT of the Portuguese Ministry of Science and Higher Education to D.P. (SFRH/BD/137487/2018).

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Copyright information

© Springer Nature Switzerland AG 2020

Authors and Affiliations

  • Maria João Freitas
    • 1
  • Daniela Patrício
    • 2
    • 3
  • Margarida Fardilha
    • 1
    Email author
  1. 1.Laboratory of Protein Phosphorylation and Proteomics, Faculty of Medicine, Department of Cellular and Molecular MedicineKU LeuvenLeuvenBelgium
  2. 2.Laboratory of Signal Transduction, Medical Sciences Department, iBiMED—Institute for Research in BiomedicineUniversity of AveiroAveiroPortugal
  3. 3.Department of Chemistry, CICECO, Aveiro Institute of MaterialsUniversity of AveiroAveiroPortugal

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